Recombinant Mouse Anti-HCV E2 Antibody (AP33)

Figure 1 Inhibition of HCV-LPs binding to cells by anti-E1 and anti-E2 antibodies.

SYTO-labeled HCV-LPs were pre-incubated with 20 to 100μg of anti-E2 (AP33) for 2h at 4°C. The HCV-LP-antibody mixtures were then incubated with Molt-4 cells for 1 h. Flow cytometry histogram of HCV-LPs binding inthe presence (20 μg/ml) (open graph) or absence (black graph) of antibodies. The background binding is shown as the gray graph.

Triyatni, M., Saunier, B., Maruvada, P., Davis, A. R., Ulianich, L., Heller, T., ... & Liang, T. J. (2002). Interaction of hepatitis C virus-like particles and cells: a model system for studying viral binding and entry. Journal of virology, 76(18), 9335-9344.

Figure 2 Neutralization of HCVpp of genotype 1a using AP33 and e509 combinations.

Increasing concentrations of AP33 alone and in combination with e509 mAb at a fixed saturating concentration (10 μg/mL). The concentration of each mAb, alone or in combination, is reported on x axis. The neutralizing activity (y axis) is expressed as percent reduction infectivity of HCVpp of genotype 1a (H77 strain) without mAbs.

Sautto, G., Mancini, N., Diotti, R. A., Solforosi, L., Clementi, M., & Burioni, R. (2012). Anti-hepatitis C virus E2 (HCV/E2) glycoprotein monoclonal antibodies and neutralization interference. Antiviral research, 96(1), 82-89.

Figure 3 Identification and characterization of mutant Jc1 and Con1/C3-neo HCVcc resistant to E2412-423-specific neutralizing antibody (AP33).

Supernatants and cells from Jc1 (squares) and Con1/C3-neo (circles) HCVcc-infected Huh7.5 cells were sequentially cultured in the absence (filled symbols) or presence (open symbols) of increasing concentrations of AP33, and HCV RNA replication was measured at various times post infection.

Pantua, H., Diao, J., Ultsch, M., Hazen, M., Mathieu, M., McCutcheon, K., ... & Hass, P. (2013). Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. Journal of molecular biology, 425(11), 1899-1914.

Figure 1 Anti-Human CEACAM5 Recombinant Antibody (PABL-496) in SDS-PAGE

SDS-PAGE analysis of PABL-496 in β-mercaptoethanol-reduced (Lane 2) and non-reduced (Lane 1) conditions.

Figure 2 Anti-Human CEACAM5 Recombinant Antibody (PABL-496) in SEC-HPLC

The purity of PABL-496 was 96.2631% as determined by SEC-HPLC.

Figure 3 Anti-Human CEACAM5 Recombinant Antibody (PABL-496) in WB

Western blot analysis of PABL-496 was performed by loading HCV E2 Protein (His Tag) protein, His tag.

Figure 4 Anti-Human CEACAM5 Recombinant Antibody (PABL-496) in ELISA

ELISA analysis of PABL-496 was performed by coating with HCV E2 Protein (His Tag). Then blocked with BSA and incubated with PABL-496. The HRP conjugated Anti-Mouse IgG as a secondary antibody (1: 2000). Detection was performed using TMB substrate and stopped with sulfuric acid. The absorbances were read on a spectrophotometer at 450 nm.